Insights into the behavior of six rationally designed peptides based on Escherichia coli's OmpA at the water-dodecane interface.

ABSTRACT: The Escherichia coli's membrane protein OmpA has been identified as a potential biosurfactant due to their amphiphilic nature, and their capacity to stabilize emulsions of dodecane in water. In this study, the influence of surfactant type, concentration, preservation time and droplet size on the crystallization of n-dodecane and water, in oil-in-water emulsions stabilized with six rationally designed Escherichia coli's OmpA-based peptides was investigated. A differential scanning calorimetry (DSC) protocol was established using emulsions stabilized with Tween 20® and Tween 80®. A relationship between the surfactant concentration and the crystallization temperatures of n-dodecane and water was observed, where the crystallization temperatures seem to be dependent on the preservation time. A

SUBMITTER: Fernandez-Nino M 

PROVIDER: S-EPMC6786535 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature